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Beta-arrestin-1 with beta-arrestin-2 shared common mechanisms to suppress podocyte autophagy by negative regulation of ATG12-ATG5 conjugation.
data suggest that beta-arr1 mediated nuclear signaling regulates the production of excretive factors derived from niche astrocytes and expansion of neural precursors in DG, thus maintaining homeostasis of adult hippocampal neurogenesis
beta-arr1 (show SAG Proteins) has a critical role in modulating ERK (show EPHB2 Proteins), JNK (show MAPK8 Proteins) and p38 MAPK (show MAPK14 Proteins) pathways mediated by TNF-alpha (show TNF Proteins) in intestinal epithelial cells.
COX-2-derived PGE2 inhibits IL-10 expression in brain microglia through a novel EP2- and beta-arrestin-dependent signaling pathway.
A specific hyaluronan-blocking peptide (Pep-1 (show CNDP2 Proteins)) has confirmed the inflammatory role of degraded hyaluronan as a mediator of the IL-1beta (show IL1B Proteins)-induced activation of beta-arrestin-1.
Data suggest that ARRB1 enhances hepatocellular carcinogenesis by inflammation-mediated Akt (show AKT1 Proteins) signaling.
Quantification of beta adrenergic receptor subtypes in beta-arrestin knockout mouse airways.
Data show that knockout or knockdown of beta-arrestin-2 (show ARRB2 Proteins) (betaarr-2), but not of beta-arrestin-1 (betaarr-1), augments beta adrenoceptor (betaAR)-stimulated cyclic AMP (show TMPRSS5 Proteins) (cAMP) production.
a neuroprotective role for ARRB1, in the context of cerebral ischemia, centered on the regulation of BECN1 (show BECN1 Proteins)-dependent autophagosome formation
results indicate that beta-arrestin1 plays a critical role in the assembly and activation of two major canonical inflammasomes
These results were consistent with those seen for beta2-AR. Thus, both beta-arrs negatively control AM1 receptor internalization, which depends on the C-tail of CLR (show DCLK3 Proteins).
Results indicate a mechanism of beta-arrestin1 in modulating epithelial-mesenchymal transition (EMT) and glycogen synthase kinase 3 beta (GSK-3beta)/beta-catenin signaling in prostate cancer, and suggest that assessment of beta-arrestin1 may provide a potential therapeutic target for prostate cancer.
The downregulation of beta-arrestins 1/2 in saphenous vein endothelial cells (SVECs) prevented the shear stress-induced rise in levels of phosphorylation of Akt (show AKT1 Proteins) and endothelial nitric oxide synthase (eNOS (show NOS3 Proteins), Serine 1177).
results suggest that ARRB1 plays an essential role in NK1R (show TACR1 Proteins)-mediated cell proliferation and G2/M transition in glioblastoma cells. Interference with ARRB1-mediated signaling via NK1R (show TACR1 Proteins) may have potential significance for therapeutic strategies targeting glioblastoma.
The beta-arrestin1.STAM1 complex is necessary for promoting autophosphorylation of focal adhesion kinase (FAK). FAK is necessary for CXCL12-induced chemotaxis and associates with and localizes with beta-arrestin1 and STAM1 in a CXCL12-dependent manner.
distinct ligands can leverage specific sequence elements on microR to regulate receptor endocytic lifetimes and the magnitude of arrestin (show SAG Proteins)-mediated signaling.
CRIP1a (show CRIP1 Proteins) can compete with beta-arrestins for interaction with C-terminal CB1R (show CNR1 Proteins) domains that could affect agonist-driven, beta-arrestin-mediated internalization of the CB1R (show CNR1 Proteins).
Low expression of ARRB1 is associated with lung cancer.
In non-small cell lung cancer patients, the loss expression of beta-arrestin1 was frequently observed, and beta-arrestin1 expression was significantly correlated with the smoking index and E-cadherin (show CDH1 Proteins) expression, which all indicated beta-arrestin1's significant clinicopathologic role
beta-arrestins regulate oxidative stress in a Nox4 (show NOX4 Proteins)-dependent manner and increase fibrosis in heart failure.
Using in vivo time-lapse imaging and three-dimensional morphology analysis of microglia in intact zebrafish larvae, study found that beta-arrestin1, a multifunctional protein involved in various signal transductions, cell-autonomously regulated the microglial morphology.
Study demonstrated that beta-arrestin1 is critically involved in zebrafish primitive hematopoiesis, where beta-arrestin1 binds to and sequesters the PcG recruiter YY1 (show YY1 Proteins), thus relieving PcG-mediated repression of cdx4-hox (show MSH2 Proteins) pathway.
The identified receptor-phospho-selective mechanism for arrestin (show SAG Proteins) conformation and the spacing of the multiple phosphate-binding sites in the arrestin (show SAG Proteins) enable arrestin (show SAG Proteins) to recognize plethora phosphorylation states of numerous GPCRs.
The presented functional map quantitatively connects critical interactions in the polar core and along the C tail of arrestin (show SAG Proteins).
Reduced binding of arrestin-1 to the phospho-opsin form of G90D mutant likely contributes to night blindness caused by this mutation.
3.0 A crystal structure of the bovine arrestin-1 splice variant p44, in which the activation step is mimicked by C-tail truncation
Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin (show SAG Proteins) activation in the desensitization process
similar to transducin activation, rhodopsin phosphorylation by GRK1 and high affinity arrestin-1 binding only requires a rhodopsin monomer
Members of arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G-protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. Arrestin beta 1 is a cytosolic protein and acts as a cofactor in the beta-adrenergic receptor kinase (BARK) mediated desensitization of beta-adrenergic receptors. Besides the central nervous system, it is expressed at high levels in peripheral blood leukocytes, and thus the BARK/beta-arrestin system is believed to play a major role in regulating receptor-mediated immune functions. Alternatively spliced transcripts encoding different isoforms of arrestin beta 1 have been described.
arrestin, beta 1
, arrestin 1
, beta-arrestin 1
, arrestin beta 1
, arrestin beta-1
, arrestin 2